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Lectin [Cleaved into: Lectin beta chain; Lectin alpha chain]

 LEC_PEA                 Reviewed;         275 AA.
P02867;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
12-SEP-2018, entry version 125.
RecName: Full=Lectin;
Contains:
RecName: Full=Lectin beta chain;
Contains:
RecName: Full=Lectin alpha chain;
Flags: Precursor;
Name=LECA; Synonyms=PSL1;
Pisum sativum (Garden pea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
50 kb inversion clade; NPAAA clade; Hologalegina; IRL clade; Fabeae;
Pisum.
NCBI_TaxID=3888;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Feltham First; TISSUE=Seed;
PubMed=3658708; DOI=10.1093/nar/15.18.7642;
Gatehouse J.A., Bown D., Evans I.M., Gatehouse L.N., Jobes D.,
Preston P., Croy R.R.D.;
"Sequence of the seed lectin gene from pea (Pisum sativum L.).";
Nucleic Acids Res. 15:7642-7642(1987).
[2]
NUCLEOTIDE SEQUENCE.
AGRICOLA=IND91054566; DOI=10.1007/BF00015881;
Kaminski P.A., Buffard D., Strosberg A.D.;
"The pea lectin gene family contains only one functional gene.";
Plant Mol. Biol. 9:497-507(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. P1/G086;
PubMed=6688253;
Higgins T.J.V., Chandler P.M., Zurawski G., Button S.C., Spencer D.;
"The biosynthesis and primary structure of pea seed lectin.";
J. Biol. Chem. 258:9544-9549(1983).
[4]
NUCLEOTIDE SEQUENCE.
STRAIN=cv. Feltham First;
de Pater B.S., Pham K.T., Katagiri F., Chua N.H., Kijne J.W.;
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 218-271.
PubMed=728447; DOI=10.1016/0005-2795(78)90514-7;
Richardson C., Behnke W.D., Freisheim J.H., Blumenthal K.M.;
"The complete amino acid sequence of the alpha-subunit of pea lectin,
Pisum sativum.";
Biochim. Biophys. Acta 537:310-319(1978).
[6]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=3782132;
Einspahr H., Parks E.H., Suguna K., Subramanian E., Suddath F.L.;
"The crystal structure of pea lectin at 3.0-A resolution.";
J. Biol. Chem. 261:16518-16527(1986).
[7]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
PubMed=8486683;
Rini J.M., Hardman K.D., Einspahr H., Suddath F.L., Carver J.P.;
"X-ray crystal structure of a pea lectin-trimannoside complex at 2.6-A
resolution.";
J. Biol. Chem. 268:10126-10132(1993).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Ruzeinikov S.N., Mikhailova I.Y., Tsygannik I.N., Pangborn W.,
Duax W., Pletnev V.Z.;
"The structure of the pea lectin-D-mannopyranose complex at a 2.1 A
resolution.";
Russ. J. Bioorg. Chem. 24:277-279(1998).
[9]
MUTAGENESIS.
PubMed=1463840; DOI=10.1007/BF00028892;
van Eijsden R.R., Hoedemaeker F.J., Diaz C.L., Lugtenberg B.J.J.,
de Pater B.S., Kijne J.W.;
"Mutational analysis of pea lectin. Substitution of Asn125 for Asp in
the monosaccharide-binding site eliminates mannose/glucose-binding
activity.";
Plant Mol. Biol. 20:1049-1058(1992).
-!- FUNCTION: D-mannose specific lectin.
-!- SUBUNIT: Tetramer of two alpha and two beta chains.
-!- MISCELLANEOUS: Binds one manganese (or another transition metal)
ion and one calcium ion. The metal ions are essential for the
saccharide-binding and cell-agglutinating activities.
-!- SIMILARITY: Belongs to the leguminous lectin family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y00440; CAA68497.1; -; Genomic_DNA.
EMBL; M18160; AAA33676.1; -; mRNA.
EMBL; J01254; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; X66368; CAA47011.1; -; Genomic_DNA.
PIR; A26844; LNPM.
PDB; 1BQP; X-ray; 2.10 A; A/C=31-211, B/D=218-264.
PDB; 1HKD; X-ray; 2.09 A; A/C=31-211, B/D=218-269.
PDB; 1OFS; X-ray; 1.80 A; A/C=31-217, B/D=218-265.
PDB; 1RIN; X-ray; 2.60 A; A/C=31-210, B/D=218-266.
PDB; 2BQP; X-ray; 1.90 A; A/B=31-264.
PDB; 2LTN; X-ray; 1.70 A; A/C=31-211, B/D=218-269.
PDB; 5T7P; X-ray; 2.16 A; A/B=31-266.
PDBsum; 1BQP; -.
PDBsum; 1HKD; -.
PDBsum; 1OFS; -.
PDBsum; 1RIN; -.
PDBsum; 2BQP; -.
PDBsum; 2LTN; -.
PDBsum; 5T7P; -.
ProteinModelPortal; P02867; -.
SMR; P02867; -.
MINT; P02867; -.
Allergome; 8818; Pis s Agglutinin.
UniLectin; P02867; -.
EvolutionaryTrace; P02867; -.
GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
CDD; cd06899; lectin_legume_LecRK_Arcelin_Co; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR016363; L-lectin.
InterPro; IPR000985; Lectin_LegA_CS.
InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
InterPro; IPR001220; Legume_lectin_dom.
Pfam; PF00139; Lectin_legB; 1.
PIRSF; PIRSF002690; L-type_lectin_plant; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
1: Evidence at protein level;
3D-structure; Calcium; Direct protein sequencing; Glycoprotein;
Lectin; Manganese; Mannose-binding; Metal-binding; Signal.
SIGNAL 1 30
CHAIN 31 217 Lectin beta chain.
/FTId=PRO_0000017623.
CHAIN 218 275 Lectin alpha chain.
/FTId=PRO_0000017624.
METAL 149 149 Manganese. {ECO:0000250}.
METAL 151 151 Calcium. {ECO:0000250}.
METAL 151 151 Manganese. {ECO:0000250}.
METAL 153 153 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 155 155 Calcium. {ECO:0000250}.
METAL 159 159 Calcium. {ECO:0000250}.
METAL 159 159 Manganese. {ECO:0000250}.
METAL 166 166 Manganese. {ECO:0000250}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 269 269 Missing (in Ref. 4). {ECO:0000305}.
STRAND 32 40 {ECO:0000244|PDB:2LTN}.
STRAND 48 52 {ECO:0000244|PDB:2LTN}.
STRAND 55 57 {ECO:0000244|PDB:1OFS}.
STRAND 58 64 {ECO:0000244|PDB:2LTN}.
STRAND 71 78 {ECO:0000244|PDB:2LTN}.
TURN 85 87 {ECO:0000244|PDB:2LTN}.
STRAND 92 102 {ECO:0000244|PDB:2LTN}.
STRAND 104 108 {ECO:0000244|PDB:1HKD}.
STRAND 112 119 {ECO:0000244|PDB:2LTN}.
HELIX 128 130 {ECO:0000244|PDB:2LTN}.
TURN 131 133 {ECO:0000244|PDB:2LTN}.
HELIX 141 143 {ECO:0000244|PDB:1OFS}.
STRAND 146 151 {ECO:0000244|PDB:2LTN}.
TURN 156 158 {ECO:0000244|PDB:2LTN}.
STRAND 166 175 {ECO:0000244|PDB:2LTN}.
STRAND 177 181 {ECO:0000244|PDB:2LTN}.
STRAND 190 197 {ECO:0000244|PDB:2LTN}.
TURN 198 201 {ECO:0000244|PDB:2LTN}.
STRAND 202 209 {ECO:0000244|PDB:2LTN}.
STRAND 219 226 {ECO:0000244|PDB:2LTN}.
HELIX 229 232 {ECO:0000244|PDB:2LTN}.
STRAND 235 244 {ECO:0000244|PDB:2LTN}.
STRAND 246 248 {ECO:0000244|PDB:1OFS}.
STRAND 251 263 {ECO:0000244|PDB:2LTN}.
SEQUENCE 275 AA; 30270 MW; FD7BE8E00A811222 CRC64;
MASLQTQMIS FYAIFLSILL TTILFFKVNS TETTSFLITK FSPDQQNLIF QGDGYTTKEK
LTLTKAVKNT VGRALYSSPI HIWDRETGNV ANFVTSFTFV INAPNSYNVA DGFTFFIAPV
DTKPQTGGGY LGVFNSAEYD KTTQTVAVEF DTFYNAAWDP SNRDRHIGID VNSIKSVNTK
SWKLQNGEEA NVVIAFNAAT NVLTVSLTYP NSLEEENVTS YTLSDVVSLK DVVPEWVRIG
FSATTGAEYA AHEVLSWSFH SELSGTSSSK QAADA


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